| IED ID | IndEnz0002012409 |
| Enzyme Type ID | protease012409 |
| Protein Name |
Thrombin-like enzyme Cdc SII SVTLE EC 3.4.21.- Fibrinogen-clotting enzyme Snake venom serine protease SVSP Fragment |
| Gene Name | |
| Organism | Crotalus durissus cumanensis (South American rattlesnake) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Crotalinae (pit vipers) Crotalus Crotalus durissus (tropical rattlesnake) Crotalus durissus cumanensis (South American rattlesnake) |
| Enzyme Sequence | VIGGDICNINEHNFLVALYE |
| Enzyme Length | 20 |
| Uniprot Accession Number | P0DKX3 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Strongly inhibited by PMSF and moderately inhibited by leupeptin. Not inhibited by EDTA, aprotinin, pepstatin, and bestatin. {ECO:0000269|PubMed:23178323}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease that coagulates human plasma and bovine fibrinogen by hydrolysis of the alpha chains (FGA) (minimum coagulation dose is 60 ug on fibrinogen). Has fibrinogenolytic activities, and degrades preferentially the Aalpha chain (FGA). Shows amidolytic activity toward N-benzoyl-L-Arg-p-nitroanilide, has a higher activity than Cdc SI. In vivo, intravenous injection induces defibrin(ogen)ation and a loss of the righting reflex and opisthotoxins, together with a typical gyroxin-like effect (18-20 minutes). Subcutaneous injection into the footpads induces moderate edema. Potentiates local hemorrhagic activity induced by metalloproteinases (BaP1). {ECO:0000269|PubMed:23178323}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (1); Domain (1); Non-terminal residue (1) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 2,234 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.145 mM for N-benzoyl-L-Arg-p-nitroanilide {ECO:0000269|PubMed:23178323}; Vmax=0.267 nmol/min/mg enzyme {ECO:0000269|PubMed:23178323}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |